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Relevant bibliographies by topics / FK-506 (Drug) – Synthesis

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Academic literature on the topic 'FK-506 (Drug) – Synthesis'

Author: Grafiati

Published: 4 June 2021

Last updated: 7 February 2022

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Journal articles on the topic "FK-506 (Drug) – Synthesis"

1

Rokaw, M. D., M. E. West, P. M. Palevsky, and J. P. Johnson. "FK-506 and rapamycin but not cyclosporin inhibit aldosterone-stimulated sodium transport in A6 cells." American Journal of Physiology-Cell Physiology 271, no. 1 (July 1, 1996): C194—C202. http://dx.doi.org/10.1152/ajpcell.1996.271.1.c194.

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The immunosuppressants cyclosporin A (CyA), FK-506, and rapamycin (RAP) have multiple actions on target cells that appear to be mediated by interaction of drug-binding protein complexes. Both FK-506 and CyA, but not RAP, inhibit the Ca2(+)-dependent phosphatase, calcineurin, and in so doing have been found to inhibit Na(+)-K(+)-ATPase activity in various nephron segments. Of interest, FK-506 and RAP, but not CyA, are bound by the steroid receptor-associated FK-506-binding heat shock protein of 56 kDa, HSP56. To determine the physiological effect of this interaction on a steroid-mediated phenomenon, the effect of these agents on steroid-mediated Na+ transport in A6 cells was investigated. Aldosterone stimulation of Na+ transport and Na(+)-K(+)-ATPase activity are significantly inhibited by prolonged incubation with FK-506 and RAP. Although CyA inhibits basal Na(+)-K(+)-ATPase activity, it has no effect on aldosterone-induced Na+ transport or the aldosterone-induced increase in Na(+)-K(+)-ATPase activity. FK-506 inhibits the aldosterone-induced synthesis of G alpha i-3 protein but has no effect on glucocorticoid receptor number as quantified by Western blotting. The results suggest that FK-506 and RAP inhibit steroid-mediated Na+ transport at some pretranslational site. The common interaction of these agents with the steroid receptor-associated HSP56 might account for these findings.

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2

White, James D., Jörg Deerberg, Steven G. Toske, and Takayuki Yakura. "Application of stereocontrolled aldol coupling to synthesis of segments of immunosuppressants FK-506 and rapamycin." Tetrahedron 65, no. 33 (August 2009): 6635–41. http://dx.doi.org/10.1016/j.tet.2009.06.030.

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3

Shevchenko, V. P., I. Yu Nagaev, N. F. Myasoedov, H. Andres, T. Moenius, and A. Susan. "Synthesis of tritiated Cyclosporin A and FK-506 by metal-catalyzed hydrogen isotope exchange." Journal of Labelled Compounds and Radiopharmaceuticals 47, no. 7 (June 2004): 407–14. http://dx.doi.org/10.1002/jlcr.827.

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4

Vannucchi, AM, A. Grossi, A. Bosi, D. Rafanelli, M. Statello, S. Guidi, R. Saccardi, and P. Rossi-Ferrini. "Effects of cyclosporin A on erythropoietin production by the human Hep3B hepatoma cell line." Blood 82, no. 3 (August 1, 1993): 978–84. http://dx.doi.org/10.1182/blood.v82.3.978.978.

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Abstract There is evidence that the inadequate erythropoietin (Epo) production observed in patients undergoing allogeneic bone marrow transplantation (BMT) might be ascribed to an inhibitory effect caused by the immunosuppressive drug cyclosporin A (CsA). In this in vitro study, we have evaluated the effects of CsA on the release of Epo in the culture medium by the human Hep3B hepatoma cell line. In cultures incubated with both CsA and the nonimmunosuppressive CsA analog MeAla-6, but not with the CsA-unrelated immunosuppressive agent FK-506, the levels of Epo in the medium were significantly reduced in comparison with controls, at concentrations (0.01 to 1.6 mumol/L) not affecting total protein synthetic rate nor the constitutive secretion of alpha- fetoprotein. Hep3B cells were found to contain a CsA-binding molecule, with an M(r) of 18 Kd, as assessed by high performance liquid chromatography (HPLC) and ligand-blotting analysis. CsA did not affect the expression of the Epo gene, as judged by Northern blot analysis, but caused a significant amount of Epo to remain unsecreted within the cells; almost all (97% of total) of the intracellular Epo was associated with the plasma membrane subcellular fraction. We conclude that: (1) CsA is able to inhibit Epo release in vitro by Hep3B cells, further supporting the hypothesis that the drug might have a role in the inappropriately low Epo levels observed in BMT patients; (2) the inhibitory effect appears to be specific and not caused by a general impairment of protein synthesis and/or secretion; and (3) the reduced Epo levels found in the medium of CsA-treated Hep3B cultures are supposed to be the consequence of an inability of the cells to correctly process Epo molecules for the secretory pathway.

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5

Vannucchi, AM, A. Grossi, A. Bosi, D. Rafanelli, M. Statello, S. Guidi, R. Saccardi, and P. Rossi-Ferrini. "Effects of cyclosporin A on erythropoietin production by the human Hep3B hepatoma cell line." Blood 82, no. 3 (August 1, 1993): 978–84. http://dx.doi.org/10.1182/blood.v82.3.978.bloodjournal823978.

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Abstract:

There is evidence that the inadequate erythropoietin (Epo) production observed in patients undergoing allogeneic bone marrow transplantation (BMT) might be ascribed to an inhibitory effect caused by the immunosuppressive drug cyclosporin A (CsA). In this in vitro study, we have evaluated the effects of CsA on the release of Epo in the culture medium by the human Hep3B hepatoma cell line. In cultures incubated with both CsA and the nonimmunosuppressive CsA analog MeAla-6, but not with the CsA-unrelated immunosuppressive agent FK-506, the levels of Epo in the medium were significantly reduced in comparison with controls, at concentrations (0.01 to 1.6 mumol/L) not affecting total protein synthetic rate nor the constitutive secretion of alpha- fetoprotein. Hep3B cells were found to contain a CsA-binding molecule, with an M(r) of 18 Kd, as assessed by high performance liquid chromatography (HPLC) and ligand-blotting analysis. CsA did not affect the expression of the Epo gene, as judged by Northern blot analysis, but caused a significant amount of Epo to remain unsecreted within the cells; almost all (97% of total) of the intracellular Epo was associated with the plasma membrane subcellular fraction. We conclude that: (1) CsA is able to inhibit Epo release in vitro by Hep3B cells, further supporting the hypothesis that the drug might have a role in the inappropriately low Epo levels observed in BMT patients; (2) the inhibitory effect appears to be specific and not caused by a general impairment of protein synthesis and/or secretion; and (3) the reduced Epo levels found in the medium of CsA-treated Hep3B cultures are supposed to be the consequence of an inability of the cells to correctly process Epo molecules for the secretory pathway.

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Dissertations / Theses on the topic "FK-506 (Drug) – Synthesis"

1

Toske, Steven Gerald. "Part I : synthesis of azetidin-2-ones from pyrazolidin-3-ones ; Part II : synthesis of a subunit of the immunosuppressant FK-506." Thesis, 1993. http://hdl.handle.net/1957/35676.

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Books on the topic "FK-506 (Drug) – Synthesis"

1

Toske, Steven Gerald. Part I: Synthesis of azetidin-2-ones from pyrazolidin-3-ones ; Part II : synthesis of a subunit of the immunosuppressant FK-506. 1993.

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Book chapters on the topic "FK-506 (Drug) – Synthesis"

1

KOCIENSKI, PHILIP, MICHAEL STOCKS, and DAVID K. DONALD. "Recent Progress in Research on the Immunosuppressant FK-506." In Chirality in Drug Design and Synthesis, 131–65. Elsevier, 1990. http://dx.doi.org/10.1016/b978-0-12-136670-4.50014-x.

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